ID   Q8YS23_NOSS1            Unreviewed;       524 AA.
AC   Q8YS23;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Serine/threonine-protein kinase B {ECO:0000256|PIRNR:PIRNR000647};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000647};
GN   OrderedLocusNames=alr3268 {ECO:0000313|EMBL:BAB74967.1};
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690 {ECO:0000313|EMBL:BAB74967.1, ECO:0000313|Proteomes:UP000002483};
RN   [1] {ECO:0000313|EMBL:BAB74967.1, ECO:0000313|Proteomes:UP000002483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576
RC   {ECO:0000313|Proteomes:UP000002483};
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000647};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|PIRNR:PIRNR000647};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PIRNR:PIRNR000647}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000019; BAB74967.1; -; Genomic_DNA.
DR   PIR; AE2214; AE2214.
DR   RefSeq; WP_010997419.1; NZ_RSCN01000001.1.
DR   AlphaFoldDB; Q8YS23; -.
DR   STRING; 103690.gene:10495306; -.
DR   KEGG; ana:alr3268; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1357; Bacteria.
DR   OrthoDB; 437733at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001646; 5peptide_repeat.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016252; Ser/Thr_kinase_SpkB.
DR   PANTHER; PTHR24363; SERINE/THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR24363:SF0; SERINE_THREONINE-PROTEIN KINASE DDB_G0277989-RELATED; 1.
DR   Pfam; PF00805; Pentapeptide; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000647; Ser/Thr_PK_SpkB; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF141571; Pentapeptide repeat-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000647, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000647, ECO:0000313|EMBL:BAB74967.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000647, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002483};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000647};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000647}.
FT   DOMAIN          34..334
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          363..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   524 AA;  57355 MW;  D4AAE36BFF924895 CRC64;
     MSYCINPTCP NPENVAFSQK CEACGSPLLL RDRYRVLKPL GQGGFGATFL AHDQILPGEP
     SCVIKQLRPS GTAPHILQMA RELFEREAKT LGTIGNHPQV PRLLDYFEEQ EQFYLVQEYI
     SGSTLQQEVK LNGTLSEPGV KQFLSEILPL LQYIHEHKVI HRDIKPANLI RRSQDARMVL
     IDFGAVKNQV SQAITNQSAN TALTAYAIGT PGFAPPEQMA MRPVYASDIY ALGITCVYLL
     TSKTPKDLDY NPTTGEVMWE HLVQASDHLI GVLRKMLEVS VRSRYQSATD VLKALEIEPY
     LESLAQGLLV KSEKEQTSQR PENSAVLSSS SPVAATSVGG VAQVAAAIRA RRAKDAAAKL
     AILPNSNSNG NGLPTQQSKA GRRLDSQTLM KAYLKGRRDF ALHNLNFLNL QGVDLSETNF
     HSAQLQSANL QGANLHNSDF GRASLTRANL KDANLNKAYF NHADLEGADL RGADLSHAYL
     SNANLRGTNL CGANLTGAKI TDEQLALAKT NWMTIRPNGK RGLL
//